Reviewed all 27 rows, including the authored inhibitor NEW. Restored conserved metal binding and immune/antibacterial terms; removed the inference that anticoagulant specialization implies loss of ancestral function. Broad negative-organismal regulation, other-organism modulation and toxin activity are compatible with the mapped prey anticoagulant role; toxin MF cannot be replaced with a BP term. Replaced unsupported exclusions of membrane/endosomal localization, iron transport, proteolysis/hydrolase activity and ossification with UNDECIDED pending root-managed focused adjudication.
Existing Falcon was read fully and its substantive bilobed iron-binding and antimicrobial evidence and sequence/activity caveat incorporated. Primary PMID:23411029 full text says: "However, it remains to be confirmed whether recombinant bat salivary lactotransferrin display anticoagulant activity." PMID:23748026 nonetheless explicitly maps the extended draculin scaffold to lactotransferrin, and curated native IXa/Xa annotations are retained. The authored inhibitor NEW is supported by this combined curated mapping and native biochemical evidence, with the same caveat; no speculative NEW was added. All source rows and their original evidence/reference fields are unchanged.
Use ferric iron binding in the core synthesis to match the explicit Fe(3+) ligand evidence; preserve the source metal-ion-binding annotation.
Removed limitation/tool-access statements from positive support where applicable and retained the actual lineage or sequence evidence. Historical uncertainties remain in the rationale rather than being treated as proof of function.
The broad GO:0046872 row is now MODIFY to GO:0008199 ferric iron binding, reflecting the conserved N-lobe Fe(3+) site while explicitly caveating the broken C-lobe iron site. Live QuickGO confirms the descendant relationship. No redundant NEW binding annotation was added; DRAFT reflects the completed review with remaining biological questions.
The focused report resolved the pending receptor-trafficking, iron-transport and protease carry-overs. Draculin retains enough of the lactotransferrin scaffold to keep metal-ion binding and serine-type peptidase activity as caveated, non-core inferences, but the C-lobe iron site and the lactoferrin protease dyad are partly degraded. Membrane/endosome locations, ion transport and broad proteolysis/hydrolase parents are now treated as over-annotations, while antibacterial and immune rows are retained as non-core family-level inferences rather than as demonstrated draculin functions.